Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.

Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily.
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DOI:
10.1016/j.str.2018.01.015
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发表时间:
2018-03-06
期刊:
Structure (London, England : 1993)
影响因子:
--
通讯作者:
Agarwal PK
Agarwal PK
中科院分区:
其他
文献类型:
--
作者:
Narayanan C;Bernard DN;Bafna K;Gagné D;Chennubhotla CS;Doucet N;Agarwal PK

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Enzyme superfamily members that share common chemical and/or biological functions also share common features. While the role of structure is well characterized, the link between enzyme function and dynamics is not well understood. We present a systematic characterization of intrinsic dynamics of over twenty members of the pancreatic-type ribonuclease (RNase) superfamily, which share a common structural fold. This study is motivated by the fact that the range of chemical activity as well as molecular motions of RNase homologs span over 105-folds. Dynamics was characterized using a combination of nuclear magnetic resonance experiments and computer simulations. Phylogenetic clustering led to the grouping of sequences into functionally distinct sub-families. Detailed characterization of the diverse RNases showed conserved dynamical traits for enzymes within sub-families. These results suggest that selective pressure for the conservation of dynamical behavior, among other factors, may be linked to the distinct chemical and biological functions in an enzyme superfamily. The pancreatic-type ribonuclease enzyme superfamily contains enzymes with diverse biological functions including angiogenesis, host defense and ribonucleolytic activity. Narayanan, Bernard et al. demonstrate that members of the family can be classified into functionally distinct subfamilies with conserved dynamical traits, which may be linked to their specific functions.
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